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O70291 (GRK4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G protein-coupled receptor kinase 4

EC=2.7.11.16
Alternative name(s):
G protein-coupled receptor kinase GRK4
Gene names
Name:Grk4
Synonyms:Gprk2l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Specifically phosphorylates the activated forms of G protein-coupled receptors.

Catalytic activity

ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate.

Enzyme regulation

Inhibited by heparin By similarity.

Subunit structure

Interacts with DRD3 By similarity.

Subcellular location

Cytoplasm. Cytoplasmcell cortex By similarity.

Post-translational modification

Palmitoylated By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Contains 1 RGS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574G protein-coupled receptor kinase 4
PRO_0000085968

Regions

Domain51 – 171121RGS
Domain186 – 448263Protein kinase
Domain449 – 51466AGC-kinase C-terminal
Nucleotide binding192 – 2009ATP By similarity
Region1 – 153153N-terminal

Sites

Active site3111Proton acceptor By similarity
Binding site2151ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict61F → M in AAC09266. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O70291 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7D7D6F46C9C044B6

FASTA57466,928
        10         20         30         40         50         60 
MELENFVANN LLLKARLGFN KQTGRSKKWR ELLKFPPVSM CTELRWSIEK DFSSLCDKQP 

        70         80         90        100        110        120 
IGRLLFRQFC DTKPDLKRCI EFLDAVAEYE VTIEEEQREF GLAIFSRFFK EKSEVPLPEI 

       130        140        150        160        170        180 
PPDIVKECKW NLKQNSPSQN VFEECAGIVC KYLSETPFEE YQESTYFNRF LQWKWLERRP 

       190        200        210        220        230        240 
VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKRILEK 

       250        260        270        280        290        300 
LHSRFVVSLA YTYETKDALC LVLTIMNGGD LKYHIYNLGD PGFEEPRAVF YAAELCCGLE 

       310        320        330        340        350        360 
DLQRKRIVYR DLKPENILLD DHGHIRISDL GLAMEVPEGE MVRGRVGTVG YMAPEIINHE 

       370        380        390        400        410        420 
KYTFSPDWWG LGCLIYEMIA GHSPFRKYKE KVNREELERR VKNETEEYSE RFSEDAKSIC 

       430        440        450        460        470        480 
SMLLIKDPSK RLGCQRDGVS AVKQHPIFKD INFSRLEANM LDPPFIPDPQ AIYCRNILDI 

       490        500        510        520        530        540 
GQFSVVKGVN LDTNDEIFYA EFATGSVTIP WQNEMIESGC FKDLNENEDD LSSLEKYKMC 

       550        560        570 
SSILRPKRNF FRRLFRRTGC LNIALSEERE PTEH 

« Hide

References

« Hide 'large scale' references
[1]"The GRK4 subfamily of G protein-coupled receptor kinases. Alternative splicing, gene organization, and sequence conservation."
Premont R.T., Macrae A.D., Aparicio S.A., Kendall H.E., Welch J.E., Lefkowitz R.J.
J. Biol. Chem. 274:29381-29389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF040745 mRNA. Translation: AAC09266.1.
AK132685 mRNA. Translation: BAE21301.1.
CH466524 Genomic DNA. Translation: EDL37466.1.
BC150691 mRNA. Translation: AAI50692.1.
RefSeqNP_001074212.1. NM_001080743.1.
NP_062370.2. NM_019497.2.
UniGeneMm.117076.

3D structure databases

ProteinModelPortalO70291.
SMRO70291. Positions 2-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000001112.

PTM databases

PhosphoSiteO70291.

Proteomic databases

PRIDEO70291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001112; ENSMUSP00000001112; ENSMUSG00000052783.
GeneID14772.
KEGGmmu:14772.
UCSCuc008xcz.1. mouse.

Organism-specific databases

CTD2868.
MGIMGI:95801. Grk4.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110512.
HOGENOMHOG000006742.
HOVERGENHBG004532.
InParanoidQ3V151.
KOK08291.
OMAHSIEKDY.
OrthoDBEOG7V1FQK.
TreeFamTF313940.

Gene expression databases

ArrayExpressO70291.
BgeeO70291.
CleanExMM_GRK4.
GenevestigatorO70291.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR00717. GPCRKINASE.
SMARTSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286867.
PROO70291.
SOURCESearch...

Entry information

Entry nameGRK4_MOUSE
AccessionPrimary (citable) accession number: O70291
Secondary accession number(s): Q3V151
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot